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P16050

- LOX15_HUMAN

UniProt

P16050 - LOX15_HUMAN

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Protein

Arachidonate 15-lipoxygenase

Gene
ALOX15, LOG15
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators. Converts arachidonic acid into 12-hydroperoxyeicosatetraenoic acid/12-HPETE and 15-hydroperoxyeicosatetraenoic acid/15-HPETE. Also converts linoleic acid to 13-hydroperoxyoctadecadienoic acid. May also act on (12S)-hydroperoxyeicosatetraenoic acid/(12S)-HPETE to produce hepoxilin A3. Probably plays an important role in the immune and inflammatory responses. Through the oxygenation of membrane-bound phosphatidylethanolamine in macrophages may favor clearance of apoptotic cells during inflammation by resident macrophages and prevent an autoimmune response associated with the clearance of apoptotic cells by inflammatory monocytes. In parallel, may regulate actin polymerization which is crucial for several biological processes, including macrophage function. May also regulate macrophage function through regulation of the peroxisome proliferator activated receptor signaling pathway. Finally, it is also involved in the cellular response to IL13/interleukin-13. Beside its role in the immune and inflammatory responses, may play a role in epithelial wound healing in the cornea maybe through production of lipoxin A4. May also play a role in endoplasmic reticulum stress response and the regulation of bone mass.2 Publications

Catalytic activityi

Arachidonate + O2 = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate.2 Publications
Arachidonate + O2 = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate.2 Publications

Cofactori

Binds 1 iron ion per subunit By similarity.

Enzyme regulationi

Activity is increased by binding phosphatidylinositol phosphates, especially phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi360 – 3601Iron; catalytic By similarity
Metal bindingi365 – 3651Iron; catalytic By similarity
Metal bindingi540 – 5401Iron; catalytic By similarity
Metal bindingi544 – 5441Iron; catalytic By similarity
Metal bindingi662 – 6621Iron; via carboxylate; catalytic By similarity

GO - Molecular functioni

  1. arachidonate 12-lipoxygenase activity Source: UniProtKB
  2. arachidonate 15-lipoxygenase activity Source: UniProtKB
  3. eoxin A4 synthase activity Source: Reactome
  4. iron ion binding Source: UniProtKB
  5. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  6. protein binding Source: UniProtKB

GO - Biological processi

  1. apoptotic cell clearance Source: UniProtKB
  2. arachidonic acid metabolic process Source: UniProtKB
  3. bone mineralization Source: UniProtKB
  4. cellular response to calcium ion Source: UniProtKB
  5. cellular response to interleukin-13 Source: UniProtKB
  6. hepoxilin biosynthetic process Source: UniProtKB
  7. inflammatory response Source: ProtInc
  8. leukotriene metabolic process Source: Reactome
  9. lipoxin A4 biosynthetic process Source: UniProtKB
  10. lipoxygenase pathway Source: UniProtKB
  11. negative regulation of adaptive immune response Source: UniProtKB
  12. ossification Source: UniProtKB
  13. phosphatidylethanolamine biosynthetic process Source: UniProtKB
  14. positive regulation of actin filament polymerization Source: UniProtKB
  15. positive regulation of cell-substrate adhesion Source: UniProtKB
  16. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  17. regulation of engulfment of apoptotic cell Source: UniProtKB
  18. regulation of peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
  19. response to endoplasmic reticulum stress Source: UniProtKB
  20. small molecule metabolic process Source: Reactome
  21. wound healing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

Calcium, Iron, Lipid-binding, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS08621-MONOMER.
ReactomeiREACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.
UniPathwayiUPA00881.

Names & Taxonomyi

Protein namesi
Recommended name:
Arachidonate 15-lipoxygenase (EC:1.13.11.33)
Short name:
15-LOX
Short name:
15-LOX-1
Alternative name(s):
12/15-lipoxygenase
Arachidonate 12-lipoxygenase, leukocyte-type (EC:1.13.11.31)
Short name:
12-LOX
Arachidonate omega-6 lipoxygenase
Gene namesi
Name:ALOX15
Synonyms:LOG15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:433. ALOX15.

Subcellular locationi

Cytoplasmcytosol. Cell membrane; Peripheral membrane protein. Lipid droplet
Note: Predominantly cytosolic; becomes enriched at membranes upon calcium binding. Translocates from the cytosol to the plasma membrane when stimulated by IL13/interleukin-13 and in macrophages binding apoptotic cells.6 Publications

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  3. lipid particle Source: UniProtKB
  4. membrane Source: UniProtKB
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Lipid droplet, Membrane

Pathology & Biotechi

Involvement in diseasei

Disease susceptibility may be associated with variations affecting the gene represented in this entry. Met at position 560 may confer interindividual susceptibility to coronary artery disease (CAD) (1 Publication).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi418 – 4181M → V: Catalyzes 15- and 12-lipoxygenation. 1 Publication

Organism-specific databases

PharmGKBiPA48.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 662661Arachidonate 15-lipoxygenasePRO_0000220697Add
BLAST

Proteomic databases

PaxDbiP16050.
PRIDEiP16050.

PTM databases

PhosphoSiteiP16050.

Expressioni

Tissue specificityi

Detected in monocytes and eosinophils (at protein level). Expressed in airway epithelial cells.2 Publications

Inductioni

Up-regulated by UV-irradiation.2 Publications

Gene expression databases

ArrayExpressiP16050.
BgeeiP16050.
CleanExiHS_ALOX15.
GenevestigatoriP16050.

Organism-specific databases

HPAiCAB004962.
CAB004963.
HPA013859.

Interactioni

Subunit structurei

Interacts with PEBP1; in response to IL13/interleukin-13, prevents the interaction of PEBP1 with RAF1 to activate the ERK signaling cascade.1 Publication

Protein-protein interaction databases

DIPiDIP-60388N.
STRINGi9606.ENSP00000293761.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ABTmodel-A2-662[»]
ProteinModelPortaliP16050.
SMRiP16050. Positions 2-662.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 114113PLATAdd
BLAST
Domaini115 – 662548LipoxygenaseAdd
BLAST

Domaini

The PLAT domain can bind calcium ions; this promotes association with membranes By similarity.

Sequence similaritiesi

Belongs to the lipoxygenase family.
Contains 1 PLAT domain.

Phylogenomic databases

eggNOGiNOG133298.
HOVERGENiHBG005150.
InParanoidiP16050.
KOiK00460.
OrthoDBiEOG7B05CG.
PhylomeDBiP16050.
TreeFamiTF105320.

Family and domain databases

Gene3Di2.60.60.20. 1 hit.
InterProiIPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view]
PANTHERiPTHR11771. PTHR11771. 1 hit.
PfamiPF00305. Lipoxygenase. 2 hits.
PF01477. PLAT. 1 hit.
[Graphical view]
PRINTSiPR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTiSM00308. LH2. 1 hit.
[Graphical view]
SUPFAMiSSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEiPS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P16050-1 [UniParc]FASTAAdd to Basket

« Hide

MGLYRIRVST GASLYAGSNN QVQLWLVGQH GEAALGKRLW PARGKETELK    50
VEVPEYLGPL LFVKLRKRHL LKDDAWFCNW ISVQGPGAGD EVRFPCYRWV 100
EGNGVLSLPE GTGRTVGEDP QGLFQKHREE ELEERRKLYR WGNWKDGLIL 150
NMAGAKLYDL PVDERFLEDK RVDFEVSLAK GLADLAIKDS LNVLTCWKDL 200
DDFNRIFWCG QSKLAERVRD SWKEDALFGY QFLNGANPVV LRRSAHLPAR 250
LVFPPGMEEL QAQLEKELEG GTLFEADFSL LDGIKANVIL CSQQHLAAPL 300
VMLKLQPDGK LLPMVIQLQL PRTGSPPPPL FLPTDPPMAW LLAKCWVRSS 350
DFQLHELQSH LLRGHLMAEV IVVATMRCLP SIHPIFKLII PHLRYTLEIN 400
VRARTGLVSD MGIFDQIMST GGGGHVQLLK QAGAFLTYSS FCPPDDLADR 450
GLLGVKSSFY AQDALRLWEI IYRYVEGIVS LHYKTDVAVK DDPELQTWCR 500
EITEIGLQGA QDRGFPVSLQ ARDQVCHFVT MCIFTCTGQH ASVHLGQLDW 550
YSWVPNAPCT MRLPPPTTKD ATLETVMATL PNFHQASLQM SITWQLGRRQ 600
PVMVAVGQHE EEYFSGPEPK AVLKKFREEL AALDKEIEIR NAKLDMPYEY 650
LRPSVVENSV AI 662
Length:662
Mass (Da):74,804
Last modified:January 23, 2007 - v3
Checksum:i9ACF7FE7863A045C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti90 – 901D → H.1 Publication
Corresponds to variant rs11568142 [ dbSNP | Ensembl ].
VAR_018746
Natural varianti102 – 1021G → V.
Corresponds to variant rs41439950 [ dbSNP | Ensembl ].
VAR_035036
Natural varianti103 – 1031N → K.1 Publication
Corresponds to variant rs11568099 [ dbSNP | Ensembl ].
VAR_018747
Natural varianti205 – 2051R → Q.1 Publication
Corresponds to variant rs11568101 [ dbSNP | Ensembl ].
VAR_018748
Natural varianti239 – 2391V → M.
Corresponds to variant rs3892408 [ dbSNP | Ensembl ].
VAR_035037
Natural varianti461 – 4611A → P.1 Publication
Corresponds to variant rs17852628 [ dbSNP | Ensembl ].
VAR_035038
Natural varianti560 – 5601T → M Loss of catalytic activity. 1 Publication
Corresponds to variant rs34210653 [ dbSNP | Ensembl ].
VAR_035039

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461E → V in AAC52118. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23892 mRNA. Translation: AAA36182.1.
U88317 Genomic DNA. Translation: AAB49305.1.
AK290309 mRNA. Translation: BAF82998.1.
AY505111 Genomic DNA. Translation: AAR84235.1.
AC118754 Genomic DNA. No translation available.
BC029032 mRNA. Translation: AAH29032.1.
U63384 Genomic DNA. Translation: AAC52118.1.
CCDSiCCDS11049.1.
PIRiA31349.
RefSeqiNP_001131.3. NM_001140.3.
UniGeneiHs.73809.

Genome annotation databases

EnsembliENST00000293761; ENSP00000293761; ENSG00000161905.
ENST00000570836; ENSP00000458832; ENSG00000161905.
GeneIDi246.
KEGGihsa:246.
UCSCiuc002fyh.3. human.

Polymorphism databases

DMDMi126396.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23892 mRNA. Translation: AAA36182.1 .
U88317 Genomic DNA. Translation: AAB49305.1 .
AK290309 mRNA. Translation: BAF82998.1 .
AY505111 Genomic DNA. Translation: AAR84235.1 .
AC118754 Genomic DNA. No translation available.
BC029032 mRNA. Translation: AAH29032.1 .
U63384 Genomic DNA. Translation: AAC52118.1 .
CCDSi CCDS11049.1.
PIRi A31349.
RefSeqi NP_001131.3. NM_001140.3.
UniGenei Hs.73809.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ABT model - A 2-662 [» ]
ProteinModelPortali P16050.
SMRi P16050. Positions 2-662.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-60388N.
STRINGi 9606.ENSP00000293761.

Chemistry

BindingDBi P16050.
ChEMBLi CHEMBL2903.
DrugBanki DB01188. Ciclopirox.
DB00179. Masoprocol.
DB00744. Zileuton.

PTM databases

PhosphoSitei P16050.

Polymorphism databases

DMDMi 126396.

Proteomic databases

PaxDbi P16050.
PRIDEi P16050.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000293761 ; ENSP00000293761 ; ENSG00000161905 .
ENST00000570836 ; ENSP00000458832 ; ENSG00000161905 .
GeneIDi 246.
KEGGi hsa:246.
UCSCi uc002fyh.3. human.

Organism-specific databases

CTDi 246.
GeneCardsi GC17M004534.
HGNCi HGNC:433. ALOX15.
HPAi CAB004962.
CAB004963.
HPA013859.
MIMi 152392. gene.
neXtProti NX_P16050.
PharmGKBi PA48.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG133298.
HOVERGENi HBG005150.
InParanoidi P16050.
KOi K00460.
OrthoDBi EOG7B05CG.
PhylomeDBi P16050.
TreeFami TF105320.

Enzyme and pathway databases

UniPathwayi UPA00881 .
BioCyci MetaCyc:HS08621-MONOMER.
Reactomei REACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_150420. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.

Miscellaneous databases

GeneWikii ALOX15.
GenomeRNAii 246.
NextBioi 979.
PROi P16050.
SOURCEi Search...

Gene expression databases

ArrayExpressi P16050.
Bgeei P16050.
CleanExi HS_ALOX15.
Genevestigatori P16050.

Family and domain databases

Gene3Di 2.60.60.20. 1 hit.
InterProi IPR008976. Lipase_LipOase.
IPR000907. LipOase.
IPR013819. LipOase_C.
IPR020834. LipOase_CS.
IPR020833. LipOase_Fe_BS.
IPR001885. LipOase_mml.
IPR001024. PLAT/LH2_dom.
[Graphical view ]
PANTHERi PTHR11771. PTHR11771. 1 hit.
Pfami PF00305. Lipoxygenase. 2 hits.
PF01477. PLAT. 1 hit.
[Graphical view ]
PRINTSi PR00087. LIPOXYGENASE.
PR00467. MAMLPOXGNASE.
SMARTi SM00308. LH2. 1 hit.
[Graphical view ]
SUPFAMi SSF48484. SSF48484. 1 hit.
SSF49723. SSF49723. 1 hit.
PROSITEi PS00711. LIPOXYGENASE_1. 1 hit.
PS00081. LIPOXYGENASE_2. 1 hit.
PS51393. LIPOXYGENASE_3. 1 hit.
PS50095. PLAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
  2. "Characterization and sequence of an additional 15-lipoxygenase transcript and of the human gene."
    Kritzik M.R., Ziober A.F., Dicharry S., Conrad D.J., Sigal E.
    Biochim. Biophys. Acta 1352:267-281(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Tongue.
  4. SeattleSNPs variation discovery resource
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-90; LYS-103 AND GLN-205.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PRO-461.
    Tissue: Brain and Lung.
  7. "Human 15-lipoxygenase gene promoter: analysis and identification of DNA binding sites for IL-13-induced regulatory factors in monocytes."
    Kelavkar U., Wang S., Montero A., Murtagh J., Shah K., Badr K.
    Mol. Biol. Rep. 25:173-182(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46.
  8. "Arachidonate 15-lipoxygenase (omega-6 lipoxygenase) from human leukocytes. Purification and structural homology to other mammalian lipoxygenases."
    Sigal E., Grunberger D., Craik C.S., Caughey G.H., Nadel J.A.
    J. Biol. Chem. 263:5328-5332(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-16.
  9. "Purification of two forms of arachidonate 15-lipoxygenase from human leukocytes."
    Izumi T., Raadmark O., Joernvall H., Samuelsson B.
    Eur. J. Biochem. 202:1231-1238(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-31; 38-45; 157-168 AND 626-631.
    Tissue: Eosinophil and Leukocyte.
  10. "A primary determinant for lipoxygenase positional specificity."
    Sloane D.L., Leung R., Craik C.S., Sigal E.
    Nature 354:149-152(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF MET-418.
  11. "Membrane translocation of 15-lipoxygenase in hematopoietic cells is calcium-dependent and activates the oxygenase activity of the enzyme."
    Brinckmann R., Schnurr K., Heydeck D., Rosenbach T., Kolde G., Kuehn H.
    Blood 91:64-74(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  12. "Evaluation of the activity and localization of 15-lipoxygenase-1 after introduction into human colorectal carcinoma Caco-2 cells."
    Hsi L.C., Kamitani H., Cornicelli J.A., Eling T.E.
    Prostaglandins Leukot. Essent. Fatty Acids 64:217-225(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. "Interaction of human 15-lipoxygenase-1 with phosphatidylinositol bisphosphates results in increased enzyme activity."
    Andersson E., Schain F., Svedling M., Claesson H.E., Forsell P.K.
    Biochim. Biophys. Acta 1761:1498-1505(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIPID-BINDING, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION.
  14. "Reciprocal regulation of 12- and 15-lipoxygenases by UV-irradiation in human keratinocytes."
    Yoo H., Jeon B., Jeon M.S., Lee H., Kim T.Y.
    FEBS Lett. 582:3249-3253(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY UV.
  15. "15(S)-Lipoxygenase-1 associates with neutral lipid droplets in macrophage foam cells: evidence of lipid droplet metabolism."
    Weibel G.L., Joshi M.R., Wei C., Bates S.R., Blair I.A., Rothblat G.H.
    J. Lipid Res. 50:2371-2376(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "15-Lipoxygenase 1 interacts with phosphatidylethanolamine-binding protein to regulate MAPK signaling in human airway epithelial cells."
    Zhao J., O'Donnell V.B., Balzar S., St Croix C.M., Trudeau J.B., Wenzel S.E.
    Proc. Natl. Acad. Sci. U.S.A. 108:14246-14251(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN IL13 SIGNALING, INTERACTION WITH PEBP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  17. Cited for: VARIANT MET-560, CHARACTERIZATION OF VARIANT MET-560, INVOLVEMENT IN CORONARY ARTERY DISEASE.

Entry informationi

Entry nameiLOX15_HUMAN
AccessioniPrimary (citable) accession number: P16050
Secondary accession number(s): A8K2P4, Q8N6R7, Q99657
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 154 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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